Abstract
Surface tension kinetics were measured for five model proteins (superoxide dismutase, cytochrome-c, myoglobin, lysozyme and ribonuclease-A) using the Wilhelmy Plate method. These data were correlated to both the stability and hydrophobicity of each protein. At low bulk concentrations, surface tension kinetics reflected the conformational stability of the protein; while at higher concentrations, surface tension kinetics were more strongly correlated with the effective hydrophobicity of the protein. The solvent accessible areas of nonpolar groups in relation with the experimental results were also discussed.
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Wei, AP., Herron, J.N., Andrade, J.D. (1990). The Role of Protein Structure in Surface Tension Kinetics. In: Crommelin, D.J.A., Schellekens, H. (eds) From Clone to Clinic. Developments in Biotherapy, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3780-5_38
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DOI: https://doi.org/10.1007/978-94-011-3780-5_38
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